arginase/ダイズ

Arginase (EC 3.5.3.1) was purified to homogeneity from cytosol of soybean, Glycine max, axes by chromatographic separations on Sephadex G-200, DEAE-sephacel, hydroxyapatite, and arginine-affinity columns. The molecular weight of the enzyme estimated by pore gradient gel electrophoresis was 240,000,

Arginase (EC 3.5.3.1) localization was studied in soybean (Glycine max L.) seedling cotyledons. Subcellular fractionation in a discontinuous Percoll gradient showed that arginase was localized in the mitochondrion. Arginine (Arg) uptake by mitochondria was demonstrated by co-sedimentation of

The effect of the inhibitor N(2)-bromoacetyl-l-ornithine (NBAO) on the biosynthesis of ornithine in higher plants, was investigated using soybean cells (Glycine max L. var Mandarin), grown in suspension culture. The NBAO was found to reduce the specific activity of the enzyme

Studies have been conducted with the arginase (l-arginine amidinohydrolase, EC 3.5.3.1) of two legumes: jack bean, Canavalia ensiformis (L.) DC., a l-canavanine-containing plant and soybean, Glycine max, a canavanine-free species. Analyses of the arginase obtained from gradient-purified mitochondria

Arginase (EC 3.5.3.1) transcript level and activity were measured in soybean (Glycine max L.) embryos from the reserve deposition stage to postgermination. Using a cDNA probe for a small soybean arginase gene family, no transcript was detected in developing embryos. However, arginase transcripts

Tracerkinetic experiments were performed using l-[guanidino-(14)C]arginine, l-[U-(14)C]arginine, l-[ureido-(14)C]citrulline, and l-[1-(14)C]ornithine to investigate arginine utilization in developing cotyledons of Glycine max (L.) Merrill. Excised cotyledons were injected with carrier-free (14)C